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Protein turnover, amino acid requirements and recommendations for athletes and active populations

Skeletal muscle is the major deposit of protein molecules. As for any cell or tissue, total muscle protein reflects a dynamic turnover between net protein synthesis and degradation. Noninvasive and invasive techniques have been applied to determine amino acid catabolism and muscle protein building a...

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Autores principales: Poortmans, J.R., Carpentier, A., Pereira-Lancha, L.O., Lancha, A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Sociedade Brasileira de Medicina Tropical 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3854183/
https://www.ncbi.nlm.nih.gov/pubmed/22666780
http://dx.doi.org/10.1590/S0100-879X2012007500096
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author Poortmans, J.R.
Carpentier, A.
Pereira-Lancha, L.O.
Lancha, A.
author_facet Poortmans, J.R.
Carpentier, A.
Pereira-Lancha, L.O.
Lancha, A.
author_sort Poortmans, J.R.
collection PubMed
description Skeletal muscle is the major deposit of protein molecules. As for any cell or tissue, total muscle protein reflects a dynamic turnover between net protein synthesis and degradation. Noninvasive and invasive techniques have been applied to determine amino acid catabolism and muscle protein building at rest, during exercise and during the recovery period after a single experiment or training sessions. Stable isotopic tracers ((13)C-lysine, (15)N-glycine, (2)H(5)-phenylalanine) and arteriovenous differences have been used in studies of skeletal muscle and collagen tissues under resting and exercise conditions. There are different fractional synthesis rates in skeletal muscle and tendon tissues, but there is no major difference between collagen and myofibrillar protein synthesis. Strenuous exercise provokes increased proteolysis and decreased protein synthesis, the opposite occurring during the recovery period. Individuals who exercise respond differently when resistance and endurance types of contractions are compared. Endurance exercise induces a greater oxidative capacity (enzymes) compared to resistance exercise, which induces fiber hypertrophy (myofibrils). Nitrogen balance (difference between protein intake and protein degradation) for athletes is usually balanced when the intake of protein reaches 1.2 g·kg(−1)·day(−1) compared to 0.8 g·kg(−1)·day(−1) in resting individuals. Muscular activities promote a cascade of signals leading to the stimulation of eukaryotic initiation of myofibrillar protein synthesis. As suggested in several publications, a bolus of 15-20 g protein (from skimmed milk or whey proteins) and carbohydrate (± 30 g maltodextrine) drinks is needed immediately after stopping exercise to stimulate muscle protein and tendon collagen turnover within 1 h.
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spelling pubmed-38541832013-12-16 Protein turnover, amino acid requirements and recommendations for athletes and active populations Poortmans, J.R. Carpentier, A. Pereira-Lancha, L.O. Lancha, A. Braz J Med Biol Res Review Skeletal muscle is the major deposit of protein molecules. As for any cell or tissue, total muscle protein reflects a dynamic turnover between net protein synthesis and degradation. Noninvasive and invasive techniques have been applied to determine amino acid catabolism and muscle protein building at rest, during exercise and during the recovery period after a single experiment or training sessions. Stable isotopic tracers ((13)C-lysine, (15)N-glycine, (2)H(5)-phenylalanine) and arteriovenous differences have been used in studies of skeletal muscle and collagen tissues under resting and exercise conditions. There are different fractional synthesis rates in skeletal muscle and tendon tissues, but there is no major difference between collagen and myofibrillar protein synthesis. Strenuous exercise provokes increased proteolysis and decreased protein synthesis, the opposite occurring during the recovery period. Individuals who exercise respond differently when resistance and endurance types of contractions are compared. Endurance exercise induces a greater oxidative capacity (enzymes) compared to resistance exercise, which induces fiber hypertrophy (myofibrils). Nitrogen balance (difference between protein intake and protein degradation) for athletes is usually balanced when the intake of protein reaches 1.2 g·kg(−1)·day(−1) compared to 0.8 g·kg(−1)·day(−1) in resting individuals. Muscular activities promote a cascade of signals leading to the stimulation of eukaryotic initiation of myofibrillar protein synthesis. As suggested in several publications, a bolus of 15-20 g protein (from skimmed milk or whey proteins) and carbohydrate (± 30 g maltodextrine) drinks is needed immediately after stopping exercise to stimulate muscle protein and tendon collagen turnover within 1 h. Sociedade Brasileira de Medicina Tropical 2012-06-08 /pmc/articles/PMC3854183/ /pubmed/22666780 http://dx.doi.org/10.1590/S0100-879X2012007500096 Text en http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License, which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Poortmans, J.R.
Carpentier, A.
Pereira-Lancha, L.O.
Lancha, A.
Protein turnover, amino acid requirements and recommendations for athletes and active populations
title Protein turnover, amino acid requirements and recommendations for athletes and active populations
title_full Protein turnover, amino acid requirements and recommendations for athletes and active populations
title_fullStr Protein turnover, amino acid requirements and recommendations for athletes and active populations
title_full_unstemmed Protein turnover, amino acid requirements and recommendations for athletes and active populations
title_short Protein turnover, amino acid requirements and recommendations for athletes and active populations
title_sort protein turnover, amino acid requirements and recommendations for athletes and active populations
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3854183/
https://www.ncbi.nlm.nih.gov/pubmed/22666780
http://dx.doi.org/10.1590/S0100-879X2012007500096
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